Evidence map›Paper›PMID 19028687›Full record

ArticleThe Journal of biological chemistry2009

PKD3 is the predominant protein kinase D isoform in mouse exocrine pancreas and promotes hormone-induced amylase secretion.

L Andy Chen, Jing Li, Scott R Silva, Lindsey N Jackson, Yuning Zhou, Hiroaki Watanabe, Kirk L Ives, Mark R Hellmich, B Mark Evers

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Protein kinase D1 - A targetable mediator of pancreatic cancer development.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  2. Protein kinase D: A therapeutic target in experimental alcoholic pancreatitis.Biochimica et biophysica acta. Molecular basis of disease · 2022
    Article
  3. Article
  4. Review
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  10. PKD signaling and pancreatitis.Journal of gastroenterology · 2016
    Review
  11. Article
  12. Protein kinase D enzymes: novel kinase targets in pancreatic cancer.Expert review of gastroenterology & hepatology · 2015
    Review
  13. Article
  14. Article
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  20. A novel protein kinase D inhibitor attenuates early events of experimental pancreatitis in isolated rat acini.American journal of physiology. Gastrointestinal and liver physiology · 2011
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

L Andy ChenDepartment of Surgery and Sealy Center for Cancer Cell Biology, The University of Texas Medical Branch, Galveston, Texas 77555-0536, USA.
Jing Li
Scott R Silva
Lindsey N Jackson
Yuning Zhou
Hiroaki Watanabe
Kirk L Ives
Mark R Hellmich
B Mark Evers
The University of Texas Medical Branch at Galveston · US

Funding

TISSUE CULTURE COREP01DK035608 · NIDDK · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI HELLMICH, MARK R · 1986 to 2010
$14.0M
SURGICAL TRAINING IN GASTROINTESTINAL ENDOCRINOLOGYT32DK007639 · NIDDK · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI RADHAKRISHNAN, RAVI S. · 1992 to 2022
$3.6M
NIDDK NIH HHS P01 DK35608NIDDK NIH HHS R01 DK48489NIDDK NIH HHS T32 DK007639
6 · The paper itself

Abstract

The protein kinase D (PKD) family of serine/threonine kinases, which can be activated by gastrointestinal hormones, consists of three distinct isoforms that modulate a variety of cellular processes including intracellular protein transport as well as constitutive and regulated secretion. Although isoform-specific functions have been identified in a variety of cell lines, the expression and function of PKD isoforms in normal, differentiated secretory tissues is unknown. Here, we demonstrate that PKD isoforms are differentially expressed in the exocrine and endocrine cells of the pancreas. Specifically, PKD3 is the predominant isoform expressed in exocrine cells of the mouse and human pancreas, whereas PKD1 and PKD2 are more abundantly expressed in the pancreatic islets. Within isolated mouse pancreatic acinar cells, PKD3 undergoes rapid membrane translocation, trans-activating phosphorylation, and kinase activation after gastrointestinal hormone or cholinergic stimulation. PKD phosphorylation in pancreatic acinar cells occurs viaaCa2+-independent, diacylglycerol- and protein kinase C-dependent mechanism. PKD phosphorylation can also be induced by physiologic concentrations of secretagogues and by in vivo stimulation of the pancreas. Furthermore, activation of PKD3 potentiates MEK/ERK/RSK (RSK, ribosomal S6 kinase) signaling and significantly enhances cholecystokinin-mediated pancreatic amylase secretion. These findings reveal a novel distinction between the exocrine and endocrine cells of the pancreas and further identify PKD3 as a signaling molecule that promotes hormone-stimulated amylase secretion.

Indexed as

AmylasesAnimalsCell LineChemokines, CCHormonesHumansIsoenzymesMaleMiceOrgan SpecificityPancreas, ExocrinePhosphorylationProtein Kinase CProtein TransportRatsSalivary GlandsAmylasesChemokines, CCHormonesIsoenzymesProtein Kinase Cprotein kinase D

Identifiers

PMID19028687
PMCPMC2629096
OpenAlexW2057870050

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.